PURIFICATION AND PROPERTIES OF KANAMYCIN-PHOSPHORYLATING ENZYME FROM PSEUDOMONAS AERUGINOSA

Publisher Website
Google Scholar
Abstract
Kanamycin-phosphorylating enzyme was extracted from Pseudomonas aeruginosa and purified by ammonium sulfate fractionation, Sephadex G-100 column and DEAE Sephadex A-50 column chromatography. This enzyme has no ATPase activity and catalyzes the reaction in which ATP reacts with kanamycin on an equimolar basis yielding kanamycin-3'-phosphate and ADP. Mg++ is required for the reaction and can be substituted with Mn++, Zn++ or Co++. The enzyme is protected from heat denaturation by the addition of kanamycin. Substrates having the specific structures of 6-amino-6-deoxy-α-D-glucopyranosyl, 2, 6-diamino-2, 6-dideoxy-α-D-glucopyranosyl or 2-amino-z-deoxy-a-D-glucopyranosyl 2-deoxystreptamines are required for the reaction. Methyl 3-amino-3-deoxy-α-D-glucopyranoside and formycin are competitive inhibitors of kanamycin and ATP respectively. Adenosine shows stronger inhibition than ADP, AMP and adenine.

This publication has 0 references indexed in Scilit: